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Q5J6J3

- DPP4_TRIRU

UniProt

Q5J6J3 - DPP4_TRIRU

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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation

pH dependencei

Optimum pH is 7.0-9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei613 – 6131Charge relay systemPROSITE-ProRule annotation
Active sitei690 – 6901Charge relay systemPROSITE-ProRule annotation
Active sitei725 – 7251Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Protein family/group databases

MEROPSiS09.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.5)
Alternative name(s):
Dipeptidyl peptidase IV
Short name:
DPP IV
Short name:
DppIV
Gene namesi
Name:DPP4
OrganismiTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifieri5551 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeTrichophyton

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 775760Dipeptidyl peptidase 4PRO_0000384089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5J6J3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5J6J3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLSLLMLA GIAQAIVPPR EPRSPTGGGN KLLTYKECVP RATISPRSTS
60 70 80 90 100
LAWINSEEDG RYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK
110 120 130 140 150
PDLSAVLWAT NYTKQYRHSY FANYFILDIK KGSLTPLAQD QAGDIQYAQW
160 170 180 190 200
SPMNNSIAYV RXNDLYIWNN GKTKRITENG GPDIFNGVPD WVYEEEIFGD
210 220 230 240 250
RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA YPRELEIRYP
260 270 280 290 300
KVSAKNPTVQ FHLLNIASSQ ETTIPVTAFP ENDLVIGEVA WLSSGHDSVA
310 320 330 340 350
YRAFNRVQDR EKIVSVKVES KESKVIRERD GTDGWIDNLL SMSYIGNVNG
360 370 380 390 400
KEYYVDISDA SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY
410 420 430 440 450
FTSTKYHSTT RHVYSVSYDT KVMTPLVNDK EAAYYTASFS AKGGYYILSY
460 470 480 490 500
QGPNVPYQEL YSTKDSKKPL KTITSNDALL EKLKEYKLPK VSFFEIKLPS
510 520 530 540 550
GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN SLDFKSYITS
560 570 580 590 600
DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKEVLKNR
610 620 630 640 650
WADKDHIGIW GXSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT
660 670 680 690 700
ERYMKTVELN ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV
710 720 730 740 750
LSNTLMNGGV TADKLTTQWF TDSDHGIRYD MDSTYQYKQL SKMVYDQKQR
760 770
RPESPPMHQW SKRVLAALFG ERAEE
Length:775
Mass (Da):88,021
Last modified:February 15, 2005 - v1
Checksum:i157774F128C6BFDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497021 Genomic DNA. Translation: AAS76665.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497021 Genomic DNA. Translation: AAS76665.1 .

3D structure databases

ProteinModelPortali Q5J6J3.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view ]
Pfami PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00131. CARBOXYPEPT_SER_SER. 1 hit.
PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum."
    Monod M., Lechenne B., Jousson O., Grand D., Zaugg C., Stoecklin R., Grouzmann E.
    Microbiology 151:145-155(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiDPP4_TRIRU
AccessioniPrimary (citable) accession number: Q5J6J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3